node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CNA1 | CNB1 | YLR433C | YKL190W | Serine/threonine-protein phosphatase 2B catalytic subunit A1; Calcineurin A; one isoform (the other is Cmp2p) of the catalytic subunit of calcineurin, a Ca++/calmodulin-regulated protein phosphatase which regulates Crz1p (a stress-response transcription factor), the other calcineurin subunit is CNB1; regulates the function of Aly1p alpha-arrestin; CNA1 has a paralog, CMP2, that arose from the whole genome duplication; Belongs to the PPP phosphatase family. PP-2B subfamily. | Calcineurin B; regulatory subunit of calcineurin, a Ca++/calmodulin-regulated type 2B protein phosphatase which regulates Crz1p (stress-response transcription factor); other calcineurin subunit encoded by CNA1 and/or CMP1; regulates function of Aly1p alpha-arrestin; myristoylation by Nmt1p reduces calcineurin activity in response to submaximal Ca signals, is needed to prevent constitutive phosphatase activity; protein abundance increases in response to DNA replication stress. | 0.999 |
CNA1 | CPR1 | YLR433C | YDR155C | Serine/threonine-protein phosphatase 2B catalytic subunit A1; Calcineurin A; one isoform (the other is Cmp2p) of the catalytic subunit of calcineurin, a Ca++/calmodulin-regulated protein phosphatase which regulates Crz1p (a stress-response transcription factor), the other calcineurin subunit is CNB1; regulates the function of Aly1p alpha-arrestin; CNA1 has a paralog, CMP2, that arose from the whole genome duplication; Belongs to the PPP phosphatase family. PP-2B subfamily. | Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A; N-terminally propionylated in vivo; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. | 0.557 |
CNA1 | FPR1 | YLR433C | YNL135C | Serine/threonine-protein phosphatase 2B catalytic subunit A1; Calcineurin A; one isoform (the other is Cmp2p) of the catalytic subunit of calcineurin, a Ca++/calmodulin-regulated protein phosphatase which regulates Crz1p (a stress-response transcription factor), the other calcineurin subunit is CNB1; regulates the function of Aly1p alpha-arrestin; CNA1 has a paralog, CMP2, that arose from the whole genome duplication; Belongs to the PPP phosphatase family. PP-2B subfamily. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.957 |
CNB1 | CNA1 | YKL190W | YLR433C | Calcineurin B; regulatory subunit of calcineurin, a Ca++/calmodulin-regulated type 2B protein phosphatase which regulates Crz1p (stress-response transcription factor); other calcineurin subunit encoded by CNA1 and/or CMP1; regulates function of Aly1p alpha-arrestin; myristoylation by Nmt1p reduces calcineurin activity in response to submaximal Ca signals, is needed to prevent constitutive phosphatase activity; protein abundance increases in response to DNA replication stress. | Serine/threonine-protein phosphatase 2B catalytic subunit A1; Calcineurin A; one isoform (the other is Cmp2p) of the catalytic subunit of calcineurin, a Ca++/calmodulin-regulated protein phosphatase which regulates Crz1p (a stress-response transcription factor), the other calcineurin subunit is CNB1; regulates the function of Aly1p alpha-arrestin; CNA1 has a paralog, CMP2, that arose from the whole genome duplication; Belongs to the PPP phosphatase family. PP-2B subfamily. | 0.999 |
CNB1 | CPR1 | YKL190W | YDR155C | Calcineurin B; regulatory subunit of calcineurin, a Ca++/calmodulin-regulated type 2B protein phosphatase which regulates Crz1p (stress-response transcription factor); other calcineurin subunit encoded by CNA1 and/or CMP1; regulates function of Aly1p alpha-arrestin; myristoylation by Nmt1p reduces calcineurin activity in response to submaximal Ca signals, is needed to prevent constitutive phosphatase activity; protein abundance increases in response to DNA replication stress. | Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A; N-terminally propionylated in vivo; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. | 0.486 |
CNB1 | CPR2 | YKL190W | YHR057C | Calcineurin B; regulatory subunit of calcineurin, a Ca++/calmodulin-regulated type 2B protein phosphatase which regulates Crz1p (stress-response transcription factor); other calcineurin subunit encoded by CNA1 and/or CMP1; regulates function of Aly1p alpha-arrestin; myristoylation by Nmt1p reduces calcineurin activity in response to submaximal Ca signals, is needed to prevent constitutive phosphatase activity; protein abundance increases in response to DNA replication stress. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema. | 0.442 |
CNB1 | FPR1 | YKL190W | YNL135C | Calcineurin B; regulatory subunit of calcineurin, a Ca++/calmodulin-regulated type 2B protein phosphatase which regulates Crz1p (stress-response transcription factor); other calcineurin subunit encoded by CNA1 and/or CMP1; regulates function of Aly1p alpha-arrestin; myristoylation by Nmt1p reduces calcineurin activity in response to submaximal Ca signals, is needed to prevent constitutive phosphatase activity; protein abundance increases in response to DNA replication stress. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.984 |
CPR1 | CNA1 | YDR155C | YLR433C | Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A; N-terminally propionylated in vivo; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. | Serine/threonine-protein phosphatase 2B catalytic subunit A1; Calcineurin A; one isoform (the other is Cmp2p) of the catalytic subunit of calcineurin, a Ca++/calmodulin-regulated protein phosphatase which regulates Crz1p (a stress-response transcription factor), the other calcineurin subunit is CNB1; regulates the function of Aly1p alpha-arrestin; CNA1 has a paralog, CMP2, that arose from the whole genome duplication; Belongs to the PPP phosphatase family. PP-2B subfamily. | 0.557 |
CPR1 | CNB1 | YDR155C | YKL190W | Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A; N-terminally propionylated in vivo; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. | Calcineurin B; regulatory subunit of calcineurin, a Ca++/calmodulin-regulated type 2B protein phosphatase which regulates Crz1p (stress-response transcription factor); other calcineurin subunit encoded by CNA1 and/or CMP1; regulates function of Aly1p alpha-arrestin; myristoylation by Nmt1p reduces calcineurin activity in response to submaximal Ca signals, is needed to prevent constitutive phosphatase activity; protein abundance increases in response to DNA replication stress. | 0.486 |
CPR1 | CPR6 | YDR155C | YLR216C | Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A; N-terminally propionylated in vivo; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | 0.526 |
CPR1 | FPR1 | YDR155C | YNL135C | Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A; N-terminally propionylated in vivo; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.987 |
CPR2 | CNB1 | YHR057C | YKL190W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema. | Calcineurin B; regulatory subunit of calcineurin, a Ca++/calmodulin-regulated type 2B protein phosphatase which regulates Crz1p (stress-response transcription factor); other calcineurin subunit encoded by CNA1 and/or CMP1; regulates function of Aly1p alpha-arrestin; myristoylation by Nmt1p reduces calcineurin activity in response to submaximal Ca signals, is needed to prevent constitutive phosphatase activity; protein abundance increases in response to DNA replication stress. | 0.442 |
CPR2 | FPR1 | YHR057C | YNL135C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.964 |
CPR3 | CPR6 | YML078W | YLR216C | Mitochondrial peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; involved in protein refolding after import into mitochondria. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | 0.503 |
CPR3 | FPR1 | YML078W | YNL135C | Mitochondrial peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; involved in protein refolding after import into mitochondria. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.980 |
CPR6 | CPR1 | YLR216C | YDR155C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A; N-terminally propionylated in vivo; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. | 0.526 |
CPR6 | CPR3 | YLR216C | YML078W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | Mitochondrial peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; involved in protein refolding after import into mitochondria. | 0.503 |
CPR6 | FPR1 | YLR216C | YNL135C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.962 |
FAP1 | FPR1 | YNL023C | YNL135C | Protein that binds to Fpr1p; confers rapamycin resistance by competing with rapamycin for Fpr1p binding; accumulates in the nucleus upon treatment of cells with rapamycin; has similarity to D. melanogaster shuttle craft and human NFX1. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.965 |
FPR1 | CNA1 | YNL135C | YLR433C | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | Serine/threonine-protein phosphatase 2B catalytic subunit A1; Calcineurin A; one isoform (the other is Cmp2p) of the catalytic subunit of calcineurin, a Ca++/calmodulin-regulated protein phosphatase which regulates Crz1p (a stress-response transcription factor), the other calcineurin subunit is CNB1; regulates the function of Aly1p alpha-arrestin; CNA1 has a paralog, CMP2, that arose from the whole genome duplication; Belongs to the PPP phosphatase family. PP-2B subfamily. | 0.957 |